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Asymmetric droplet interface bilayers.

William L Hwang1, Min Chen, Bríd Cronin

  • 1Chemistry Research Laboratory, Department of Chemistry, University of Oxford, OX1 3TA, England, UK. william.hwang@chem.ox.ac.uk

Journal of the American Chemical Society
|April 15, 2008
PubMed
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Asymmetric droplet interface bilayers (a-DIBs) were developed to mimic cell membrane leaflet differences. This new model system allows for single-channel electrical recording of membrane proteins, revealing differences in their activity based on bilayer composition.

Area of Science:

  • Biophysics
  • Membrane Biology
  • Nanotechnology

Background:

  • Cell membranes possess distinct lipid compositions in their inner and outer leaflets.
  • Existing model systems often lack the asymmetry required to accurately mimic native membrane environments.
  • Droplet interface bilayers (DIBs) offer a platform for electrical recording but typically use symmetric compositions.

Purpose of the Study:

  • To develop a robust model system for single-channel electrical recording of membrane proteins in asymmetric lipid bilayers.
  • To investigate the influence of leaflet composition on membrane protein behavior using a novel asymmetric DIB (a-DIB) system.
  • To enable the study of ion channels and pores in environments that more closely resemble native cell membranes.

Main Methods:

Related Experiment Videos

  • Formation of asymmetric DIBs (a-DIBs) by incorporating lipid vesicles of varying compositions into aqueous droplets within an oil bath.
  • Insertion and functional assessment of both alpha-helical and beta-barrel membrane proteins within the a-DIBs.
  • Single-channel electrical recording to measure the activity and gating behavior of membrane proteins.

    • Main Results:

    • Demonstrated successful insertion and functional recording of membrane proteins in a-DIBs.
    • Observed distinct gating behavior for Outer membrane protein G (OmpG) from Escherichia coli when inserted into a-DIBs with opposing charged leaflets (positive vs. negative).
    • Validated the a-DIB system as a versatile platform for studying leaflet-specific effects on protein function.

    Conclusions:

    • The developed asymmetric DIB (a-DIB) system effectively mimics the compositional asymmetry of cell membrane leaflets.
    • a-DIBs facilitate the study of membrane protein function, including gating properties, under physiologically relevant asymmetric conditions.
    • This platform provides new opportunities to explore how bilayer asymmetry impacts the behavior of membrane proteins like ion channels and pores.